ID   P5CS2_ARATH             Reviewed;         726 AA.
AC   P54888; Q9M061;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-DEC-2008, entry version 68.
DE   RecName: Full=Delta-1-pyrroline-5-carboxylate synthetase B;
DE            Short=P5CS B;
DE   Includes:
DE     RecName: Full=Glutamate 5-kinase;
DE              Short=GK;
DE              EC=2.7.2.11;
DE     AltName: Full=Gamma-glutamyl kinase;
DE   Includes:
DE     RecName: Full=Gamma-glutamyl phosphate reductase;
DE              Short=GPR;
DE              EC=1.2.1.41;
DE     AltName: Full=Glutamate-5-semialdehyde dehydrogenase;
DE     AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase;
GN   Name=P5CSB; Synonyms=P5CS2; OrderedLocusNames=At3g55610;
GN   ORFNames=F1I16_20;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9351242; DOI=10.1046/j.1365-313X.1997.00557.x;
RA   Strizhov N., Abraham E., Oekresz L., Blickling S., Zilberstein A.,
RA   Schell J., Koncz C., Szabados L.;
RT   "Differential expression of two P5CS genes controlling proline
RT   accumulation during salt-stress requires ABA and is regulated by ABA1,
RT   ABI1 and AXR2 in Arabidopsis.";
RL   Plant J. 12:557-569(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: P5CS plays a key role in proline biosynthesis, leading
CC       to osmoregulation in plants.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate = ADP + L-glutamate 5-
CC       phosphate.
CC   -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate +
CC       NADP(+) = L-glutamyl 5-phosphate + NADPH.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-glutamate: step 1/2.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-glutamate: step 2/2.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences;
CC       Name=1;
CC         IsoId=P54888-1; Sequence=Displayed;
CC   -!- SIMILARITY: In the N-terminal section; belongs to the glutamate 5-
CC       kinase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the gamma-
CC       glutamyl phosphate reductase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB81586.1; Type=Erroneous gene model prediction;
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DR   EMBL; X86778; CAA60447.1; -; Genomic_DNA.
DR   EMBL; Y09355; CAA70527.1; -; mRNA.
DR   EMBL; AL161667; CAB81586.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY091766; AAM10314.1; -; mRNA.
DR   PIR; T47700; T47700.
DR   PIR; T50682; T50684.
DR   RefSeq; NP_191120.2; -.
DR   UniGene; At.25196; -.
DR   HSSP; Q9WYC9; 1O20.
DR   PRIDE; P54888; -.
DR   GeneID; 824727; -.
DR   GenomeReviews; BA000014_GR; AT3G55610.
DR   NMPDR; fig|3702.1.peg.16879; -.
DR   TAIR; At3g55610; -.
DR   ArrayExpress; P54888; -.
DR   GermOnline; AT3G55610; Arabidopsis thaliana.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0004349; F:glutamate 5-kinase activity; IEA:InterPro.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase acti...; IEA:InterPro.
DR   GO; GO:0009793; P:embryonic development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR   InterPro; IPR016163; Ald_DHase_C.
DR   InterPro; IPR016162; Ald_DHase_N.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR000965; Gglut_pp_reduct.
DR   InterPro; IPR001057; Glu_5kinase.
DR   InterPro; IPR005766; P5_carboxy_syn.
DR   InterPro; IPR005715; ProB.
DR   Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1.
DR   Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF036429; P5C_syn; 1.
DR   PRINTS; PR00474; GLU5KINASE.
DR   TIGRFAMs; TIGR01092; P5CS; 1.
DR   TIGRFAMs; TIGR00407; proA; 1.
DR   TIGRFAMs; TIGR01027; proB; 1.
DR   PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR   PROSITE; PS01223; PROA; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Amino-acid biosynthesis; Complete proteome;
KW   Kinase; Multifunctional enzyme; NADP; Oxidoreductase;
KW   Proline biosynthesis; Transferase.
FT   CHAIN         1    726       Delta-1-pyrroline-5-carboxylate
FT                                synthetase B.
FT                                /FTId=PRO_0000109773.
FT   REGION        1    296       Glutamate 5-kinase.
FT   REGION      297    717       Gamma-glutamyl phosphate reductase.
SQ   SEQUENCE   726 AA;  78871 MW;  E01446A6659021FF CRC64;
     MTEIDRSRAF AKDVKRIVVK VGTAVVTGKG GRLALGRLGA ICEQLAELNS DGFEVILVSS
     GAVGLGRQRL RYRQLVNSSF ADLQKPQMEL DGKACAGVGQ SSLMAYYETM FDQLDVTVAQ
     MLVTDSSFRD KDFRKQLSET VKAMLRMRVI PVFNENDAIS TRRAPYKDST GIFWDNDSLA
     ALLSLELKAD LLILLSDVEG LYTGPPSDST SKLIHTFIKE KHQDEITFGE KSKLGRGGMT
     AKVKAAVNAA YGGVPVIITS GYAAENISKV LRGLRVGTLF HQDAHLWAPV VDTTSRDMAV
     AARESSRKLQ ALSSEDRKQI LHDIANALEV NEKTIKAEND LDVAAAQEAG YEESLVARLV
     MKPGKISSLA ASVRQLAEME DPIGRVLKKT QVADDLILEK TSSPIGVLLI VFESRPDALV
     QIASLAIRSG NGLLLKGGKE ARRSNAILHK VITDAIPETV GGKLIGLVTS REEIPDLLKL
     DDVIDLVIPR GSNKLVSQIK NSTKIPVLGH ADGICHVYVD KSGKLDMAKR IVSDAKLDYP
     AACNAMETLL VHKDLEQNGF LDDLIYVLQT KGVTLYGGPR ASAKLNIPET KSFHHEYSSK
     ACTVEIVEDV YGAIDHIHQH GSAHTDCIVT EDSEVAEIFL RQVDSAAVFH NASTRFSDGF
     RFGLGAEVGI STSRIHARGP VGVEGLLTTR WIMRGKGQVV DGDNGIVYTH KDLPVLQRTE
     AVENGI
//